EC Number |
Metals/Ions |
Reference |
---|
1.11.1.5 | Ca2+ |
a single, tightly bound, Ca2+ ion at the domain interface of both the fully oxidized and mixed-valence forms of the enzyme is absolutely required for catalytic activity, reduction of the electron-transferring (high-potential) heme in the presence of Ca2+ ions triggers substantial structural rearrangements around the active-site (low-potential) heme to allow substrate binding and catalysis |
685208 |
1.11.1.5 | Ca2+ |
pre-incubation with the cation has no effect on activity |
659522 |
1.11.1.5 | Ca2+ |
with added Ca2+, the peroxidatic heme is five-coordinate high-spin and active |
685251 |
1.11.1.5 | Fe |
2 hemes |
663999 |
1.11.1.5 | Fe |
2 hemes per subunit |
664002 |
1.11.1.5 | Fe |
static titration of ferric cytochrome c peroxidase with reduced azurin shows that only one of the two hemes in the enzyme seems to be readily reduced |
665456 |
1.11.1.5 | Fe |
two haeme groups |
663918 |
1.11.1.5 | Fe |
two haemes per monomer, pyridine haemochrome spectra |
394632 |
1.11.1.5 | Fe2+ |
diheme cytochrome c peroxidase |
724008 |
1.11.1.5 | Fe2+ |
heme |
724658 |